Phosphatase Subfamily ACP5 - Revision history

Gerard at 16:27, 15 May 2016

2016-05-15T16:27:38Z

Gerard: /* Functions */

2016-05-15T16:26:52Z

‎Functions

Gerard at 16:26, 15 May 2016

2016-05-15T16:26:36Z

Gerard at 16:02, 15 May 2016

2016-05-15T16:02:35Z

Gerard: /* Function */

2016-05-15T15:41:26Z

‎Function

Gerard: /* Evolution */

2016-05-15T15:26:15Z

‎Evolution

Gerard: /* References */

2016-05-15T15:21:46Z

‎References

Gerard: /* Evolution */

2016-05-15T15:15:53Z

‎Evolution

Gerard at 15:09, 15 May 2016

2016-05-15T15:09:28Z

Gerard: /* Evolution */

2016-05-15T15:05:00Z

‎Evolution

@@ Line 2: / Line 2: @@
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_PPPL|Fold PPPL]]: [[Phosphatase_Superfamily_PPPL|Superfamily PPPL]]: [[Phosphatase_Family_PAP|Family PAP]]: [[Phosphatase_Subfamily_ACP5|ACP5]]
-ACP5 is found in most eukaryotes. It removes the mannose-6-phosphate trafficking signal in lysosomal proteins and is also reported to have protein substrates, including osteopontin.
+ACP5 is found in most eukaryotes. It removes the mannose-6-phosphate trafficking signal in lysosomal proteins and is also a secreted protein phosphatase acting on osteopontin and other secreted proteins.
 === Evolution ===

@@ Line 17: / Line 17: @@
 ACP5 dephosphorylates mannose 6-phosphate (M6P) modification on lysosomal proteins. Most newly synthesized lysosomal proteins are labelled with M6P by a Golgi-resisdent phosphotransferase. This modification is recognized by receptors that target the lysosomal proteins to the lysosome where, in most cell types, the M6P recognition marker is rapidly removed <cite>sun08</cite>. This function is shared by the unrelated phosphatase [[Phosphatase_Subfamily_ACP2|ACP2]]. The loss of the ACP5 subfamily in yeast may parallel their lack of M6P-based sorting <cite>Li</cite>, though plants are also believed to lack M6P sorting, yet have ACP5 members.
-Human ACP5  also acts as an osteopontin phosphatase <cite>andersson03</cite>. [http://en.wikipedia.org/wiki/Osteopontin Osteopontin] is an extracellular phosphoprotein involved in biomineralization and bone remodeling, as well as immune functions in heart, chemotaxis, cell activation, apoptosis. It is phosphorylated by the Golgi-resident kinase, [http://kinase.com/wiki/index.php/Kinase_Family_GASK FAM20]. ACP5 modulates the ability of osteopontin to cause osteoclast migration <cite>Ek-Rylander</cite> ACP5 is also secreted and may have roles in dendritic cell and macrophage activation<cite>Esfandiari, Raisanen</cite>, fetal erythropoesis <cite>Ying</cite> and adipogenesis <cite>Lang</cite>. Other reported ACP substrates include osteonectin, bone sialoprotein, gastrin, and casein<cite><Andersson95</cite>.
+Human ACP5  also acts as an osteopontin phosphatase <cite>andersson03</cite>. [http://en.wikipedia.org/wiki/Osteopontin Osteopontin] is an extracellular phosphoprotein involved in biomineralization and bone remodeling, as well as immune functions in heart, chemotaxis, cell activation, apoptosis. It is phosphorylated by the Golgi-resident kinase, [http://kinase.com/wiki/index.php/Kinase_Family_GASK FAM20]. ACP5 modulates the ability of osteopontin to cause osteoclast migration <cite>Ek-Rylander</cite> ACP5 is also secreted and may have roles in dendritic cell and macrophage activation <cite>Esfandiari, Raisanen</cite>, fetal erythropoesis <cite>Ying</cite> and adipogenesis <cite>Lang</cite>. Other reported ACP substrates include osteonectin, bone sialoprotein, gastrin, and casein<cite><Andersson95</cite>.
-−
-−
 === References ===

@@ Line 17: / Line 17: @@
 ACP5 dephosphorylates mannose 6-phosphate (M6P) modification on lysosomal proteins. Most newly synthesized lysosomal proteins are labelled with M6P by a Golgi-resisdent phosphotransferase. This modification is recognized by receptors that target the lysosomal proteins to the lysosome where, in most cell types, the M6P recognition marker is rapidly removed <cite>sun08</cite>. This function is shared by the unrelated phosphatase [[Phosphatase_Subfamily_ACP2|ACP2]]. The loss of the ACP5 subfamily in yeast may parallel their lack of M6P-based sorting <cite>Li</cite>, though plants are also believed to lack M6P sorting, yet have ACP5 members.
-Human ACP5  also acts as an osteopontin phosphatase <cite>andersson03</cite>. [http://en.wikipedia.org/wiki/Osteopontin Osteopontin] is an extracellular phosphoprotein involved in biomineralization and bone remodeling, as well as immune functions in heart, chemotaxis, cell activation, apoptosis. It is phosphorylated by the Golgi-resident kinase, [http://kinase.com/wiki/index.php/Kinase_Family_GASK FAM20].
+Human ACP5  also acts as an osteopontin phosphatase <cite>andersson03</cite>. [http://en.wikipedia.org/wiki/Osteopontin Osteopontin] is an extracellular phosphoprotein involved in biomineralization and bone remodeling, as well as immune functions in heart, chemotaxis, cell activation, apoptosis. It is phosphorylated by the Golgi-resident kinase, [http://kinase.com/wiki/index.php/Kinase_Family_GASK FAM20]. ACP5 modulates the ability of osteopontin to cause osteoclast migration <cite>Ek-Rylander</cite> ACP5 is also secreted and may have roles in dendritic cell and macrophage activation<cite>Esfandiari, Raisanen</cite>, fetal erythropoesis <cite>Ying</cite> and adipogenesis <cite>Lang</cite>. Other reported ACP substrates include osteonectin, bone sialoprotein, gastrin, and casein<cite><Andersson95</cite>.
@@ Line 23: / Line 23: @@
 === References ===
 <biblio>
 #andersson03 pmid=14584906
 #Guddat99 pmid=10425678
 #Li pmid=18786576
 #sun08 pmid=18940929
 #Uppenberg99 pmid=10388567
 </biblio>

@@ Line 14: / Line 14: @@
 ACP5 has a [[HMM_PD0127|purple acid phosphatase N-terminal domain]], a phosphatase domain, and [http://pfam.xfam.org/family/Metallophos_C purple acid phosphatase C-terminal domain]. The boundary of the phosphatase domain is defined according to the crystal structures <cite> Uppenberg99, Guddat99</cite>.
-=== Function ===
+=== Functions ===
-Human ACP5 hydrolyzes a variety of phosphomonoesters at acid pH ''in vitro''. ACP5 also acts as an osteopontin phosphatase <cite>andersson03</cite>. [http://en.wikipedia.org/wiki/Osteopontin Osteopontin] is a protein that in humans is encoded by the SPP1 gene (secreted phosphoprotein 1). Osteopontin is involved in many biological processes including biomineralization, bone remodeling, immune functions in heart, chemotaxis, cell activation, apoptosis.
+ACP5 dephosphorylates mannose 6-phosphate (M6P) modification on lysosomal proteins. Most newly synthesized lysosomal proteins are labelled with M6P by a Golgi-resisdent phosphotransferase. This modification is recognized by receptors that target the lysosomal proteins to the lysosome where, in most cell types, the M6P recognition marker is rapidly removed <cite>sun08</cite>. This function is shared by the unrelated phosphatase [[Phosphatase_Subfamily_ACP2|ACP2]]. The loss of the ACP5 subfamily in yeast may parallel their lack of M6P-based sorting <cite>Li</cite>, though plants are also believed to lack M6P sorting, yet have ACP5 members.
 === References ===

@@ Line 17: / Line 17: @@
 Human ACP5 hydrolyzes a variety of phosphomonoesters at acid pH ''in vitro''. ACP5 also acts as an osteopontin phosphatase <cite>andersson03</cite>. [http://en.wikipedia.org/wiki/Osteopontin Osteopontin] is a protein that in humans is encoded by the SPP1 gene (secreted phosphoprotein 1). Osteopontin is involved in many biological processes including biomineralization, bone remodeling, immune functions in heart, chemotaxis, cell activation, apoptosis.
-ACP5 also dephosphorylates mannose 6-phosphate (M6P) modification on lysosomal proteins. Most newly synthesized lysosomal proteins are labelled with M6P by a Golgi-resisdent phosphotransferase. This modification is recognized by receptors that target the lysosomal proteins to the lysosome where, in most cell types, the M6P recognition marker is rapidly removed <cite>sun08</cite>. This function is shared by the unrelated phosphatase [[Phosphatase_Subfamily_ACP2|ACP2]].
+ACP5 also dephosphorylates mannose 6-phosphate (M6P) modification on lysosomal proteins. Most newly synthesized lysosomal proteins are labelled with M6P by a Golgi-resisdent phosphotransferase. This modification is recognized by receptors that target the lysosomal proteins to the lysosome where, in most cell types, the M6P recognition marker is rapidly removed <cite>sun08</cite>. This function is shared by the unrelated phosphatase [[Phosphatase_Subfamily_ACP2|ACP2]]. The loss of the ACP5 subfamily in yeast may parallel their lack of M6P-based sorting <cite>Li</cite>, though plants are also believed to lack M6P sorting, yet have ACP5 members.
 === References ===

@@ Line 5: / Line 5: @@
 === Evolution ===
-ACP5 is present in some prokaryotes, and most eukaryotes, though absent from many fungi, which lack mannose-6-phosphate lysosomal targetting <cite>Li</cite>. ACP5 subfamily has a single member in human genome, which is also called tartrate resistant acid phosphatase (TRAP) or uteroferrin. Fruit fly has a single ACP5 gene (CG1637), which encodes at least five protein isoforms. C. elegans, nematostella, sponge, Monosiga and Dictyostelium have multiple ACP5 genes; some are chromosomal neighbors, indicating recent duplication..
+ACP5 is present in some prokaryotes, and most eukaryotes, though absent from many fungi, which lack mannose-6-phosphate lysosomal targetting <cite>Li</cite>. The single human member, ACP5 is also called tartrate resistant acid phosphatase (TRAP) or uteroferrin. Fruit fly has a single ACP5 gene (CG1637), which encodes at least five protein isoforms. C. elegans, Nematostella, sponge, Monosiga and Dictyostelium have multiple ACP5 genes; some are chromosomal neighbors, indicating recent duplication.
 One Monosiga ACP5 ([[Phosphatase_Sequence_MbreP089_AA]]) has an additional SapB (Sphingolipid Activator Protein, B) domain. The unusual domain combination is also found in ''Salpingoeca rosetta'', ''Capsaspora owczarzaki'' and ''Thecamonas trahens'', suggesting it probably emerged in the common ancestor between Apusomonadida and Opisthokonta. The human SapB, produced by the cleavage of [https://en.wikipedia.org/wiki/Prosaposin human PSAP gene] activates many enzymes through interaction with the substrates.

@@ Line 1: / Line 1: @@
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_PPPL|Fold PPPL]]: [[Phosphatase_Superfamily_PPPL|Superfamily PPPL]]: [[Phosphatase_Family_PAP|Family PAP]]: [[Phosphatase_Subfamily_ACP5|ACP5]]
-__NOTOC__
+ACP5 is found in most eukaryotes. It removes the mannose-6-phosphate trafficking signal in lysosomal proteins and is also reported to have protein substrates, including osteopontin.
-−
-ACP5 subfamily is found in most eukaryotes. Human ACP5 hydrolyzes a variety of phosphomonoesters at acid pH in vitro. It also show phosphatase activity towards protein osteopontin, and mannose 6-phosphate modification on lysosomal proteins.
 === Evolution ===
-ACP5 is present in most eukaryotic groups, such as animals and plants. It is found in few fungi, though. ACP5 is also observed in some prokaryotes. ACP5 subfamily has a single member in human genome, which is also called tartrate resistant acid phosphatase (TRAP) or uteroferrin. Fruit fly has a single ACP5 gene (CG1637), which encodes at least five protein isoforms. C. elegans, nematostella, sponge, monosiga and dicty have multiple ACP5 genes; some but not all locate close to each other, even in the form of tandem duplications.
+ACP5 is present in some prokaryotes, and most eukaryotes, though absent from many fungi. ACP5 subfamily has a single member in human genome, which is also called tartrate resistant acid phosphatase (TRAP) or uteroferrin. Fruit fly has a single ACP5 gene (CG1637), which encodes at least five protein isoforms. C. elegans, nematostella, sponge, Monosiga and Dictyostelium have multiple ACP5 genes; some are chromosomal neighbors, indicating recent duplication..
 One Monosiga ACP5 ([[Phosphatase_Sequence_MbreP089_AA]]) has an additional SapB (Sphingolipid Activator Protein, B) domain. The unusual domain combination is also found in ''Salpingoeca rosetta'', ''Capsaspora owczarzaki'' and ''Thecamonas trahens'', suggesting it probably emerged in the common ancestor between Apusomonadida and Opisthokonta. The human SapB, produced by the cleavage of [https://en.wikipedia.org/wiki/Prosaposin human PSAP gene] activates many enzymes through interaction with the substrates.
-Another Monosiga ACP5 ([[Phosphatase_Sequence_MbreP088_AA]]) has an additional GBP (Guanylate-binding protein) domain; One of nematostella ACP5 has two tandem phosphatase domains. However, the two domain combinations are found only in ''Monosiga brevicollis'' and ''Nematostella vectensis'', respectively.
+Another Monosiga ACP5 ([[Phosphatase_Sequence_MbreP088_AA]]) has an additional GBP (Guanylate-binding protein) domain; One Nematostella ACP5 has two tandem phosphatase domains. Neither of these domain combinations are conserved, and may be gene prediction artefacts.
 === Domain ===